ID F4CY30_PSEUX Unreviewed; 466 AA.
AC F4CY30;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN OrderedLocusNames=Psed_2046 {ECO:0000313|EMBL:AEA24271.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA24271.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA24271.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000018,
CC ECO:0000256|RuleBase:RU361171};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP002593; AEA24271.1; -; Genomic_DNA.
DR RefSeq; WP_013674202.1; NC_015312.1.
DR AlphaFoldDB; F4CY30; -.
DR STRING; 675635.Psed_2046; -.
DR KEGG; pdx:Psed_2046; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_019582_2_2_11; -.
DR OMA; VGWVFWR; -.
DR OrthoDB; 3401800at2; -.
DR Proteomes; UP000007809; Chromosome.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.160; -; 1.
DR Gene3D; 4.10.280.50; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010107; Glutamate_decarboxylase.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT MOD_RES 274
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 466 AA; 51770 MW; D26CE39EB1F7EFB0 CRC64;
MPLHDRDTVR DELDDCVFVD RDLTRPVTKY RFPQEESLPR DVSQLVSDEL MLDGNARQNL
ATFCQTWVEP EVMGLMALSV SKNMIDKDEY PQTAEIERRC VHMMADLWNA PEAANTVGAS
AIGSSEACML AGMAAKWRWR AKRRAAGKPV DNPNMVCGPV QVVWHKFARY WDIEMREVPM
APGSYAMDAA SMLERVDENT IMVVPTLGVT YTGAYEPVAD MALALDQLQA DTGLDVDIHV
DAASGGFLAP FCAPDLAFDF RLPRVKSISA SGHKFGLAPL GVGWVVWRGA GELPDDLVFH
VNYLGGDMPV FQINFSRPAG QIVASYYNFL RLGREGYRRI HDASYDVGQY LAAEIVKLGP
FELLCDSRPD TGIPTVTWRI REGEDPGYTL YDLADRLRTK GWQVPAYTLT GTASDIAVQR
ILVRLGVSRD MASLLLDDFR DAVAHFGKHP VTIPMTKQES GGFSHL
//